Spacer Domain in Hepatitis B Virus Polymerase: Plugging a Hole or Performing a Role?
MetadataShow full item record
Pley, C., Lourenço, J., McNaughton, A. L., & Matthews, P. C. (2022). Spacer Domain in Hepatitis B Virus Polymerase: Plugging a Hole or Performing a Role?. J Virol, 96 (9) https://doi.org/10.1128/jvi.00051-22
Funder: NIHR | NIHR Oxford Biomedical Research Centre
Funder: NIHR | NIHR Oxford Biomedical Research Centre (OxBRC)
Hepatitis B virus (HBV) polymerase is divided into terminal protein, spacer, reverse transcriptase, and RNase domains. Spacer has previously been considered dispensable, merely acting as a tether between other domains or providing plasticity to accommodate deletions and mutations. We explore evidence for the role of spacer sequence, structure, and function in HBV evolution and lineage, consider its associations with escape from drugs, vaccines, and immune responses, and review its potential impacts on disease outcomes.
Polymorphism, Evolution, Genotype, Hepatitis B virus, Phylogeny, Diversity, HBV, Polymerase, Spacer
Wellcome Trust (110110/Z/15/Z)
External DOI: https://doi.org/10.1128/jvi.00051-22
This record's URL: https://www.repository.cam.ac.uk/handle/1810/337158
Attribution 4.0 International
Licence URL: https://creativecommons.org/licenses/by/4.0/